English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Resequencing estA3, an allele of the methanol-soluble heat-stable enterotoxin of Escherichia coli showed that the proline triplet 19 is in fact an alanine codon; thus, estA alleles 3 and 4 were shown to be identical. Resequencing has also shown that the carboxy terminus of another allele, estA2, is not the previously inferred histidine triplet but the same tyrosine codon reported for all other estA alleles. The improperly inferred histidine codon was used in constructions to fuse estA2 to the B subunit of the heat-labile enterotoxin gene, and the fused gene products as well as three amino acid insertional mutants containing histidine-72 were not efficiently secreted. We show that the defective secretion is not due to histidine as a carboxy-terminal residue, since site-directed mutagenesis of wild-type tyrosine-72 to histidine did not influence the localization of the activity of the methanol-soluble heat-stable enterotoxin.

infection and immunity

Rectification of two Escherichia coli heat-stable enterotoxin allele sequences and lack of biological effect of changing the carboxy-terminal tyrosine to histidine